4fnp: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4fnp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FNP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FNP FirstGlance]. <br>
<table><tr><td colspan='2'>[[4fnp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FNP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FNP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.803&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fnp OCA], [https://pdbe.org/4fnp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fnp RCSB], [https://www.ebi.ac.uk/pdbsum/4fnp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fnp ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fnp OCA], [https://pdbe.org/4fnp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fnp RCSB], [https://www.ebi.ac.uk/pdbsum/4fnp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fnp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/AGAA_GEOSE AGAA_GEOSE] Hydrolyzes the short-chain alpha-galactosaccharides raffinose and stachyose.<ref>PMID:23012371</ref>  
[https://www.uniprot.org/uniprot/AGAA_GEOSE AGAA_GEOSE] Hydrolyzes the short-chain alpha-galactosaccharides raffinose and stachyose.<ref>PMID:23012371</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The alpha-galactosidase AgaA from the thermophilic microorganism Geobacillus stearothermophilus has great industrial potential because it is fully active at 338 K against raffinose and can increase the yield of manufactured sucrose. AgaB has lower affinity for its natural substrates but is a powerful tool for the enzymatic synthesis of disaccharides by transglycosylation. These two enzymes have 97% identity and belong to the glycoside hydrolase (GH) family GH36 for which few structures are available. To understand the structural basis underlying the differences between these two enzymes, we determined the crystal structures of AgaA and AgaB by molecular replacement at 3.2- and 1.8 A-resolution, respectively. We also solved a 2.8-A structure of the AgaA(A355E) mutant, which has enzymatic properties similar to those of AgaB. We observe that residue 355 is located 20 A away from the active site and that the A355E substitution causes structural rearrangements resulting in a significant displacement of the invariant Trp(336) at catalytic subsite -1. Hence, the active cleft of AgaA is narrowed in comparison with AgaB, and AgaA is more efficient than AgaB against its natural substrates. The structure of AgaA(A355E) complexed with 1-deoxygalactonojirimycin reveals an induced fit movement; there is a rupture of the electrostatic interaction between Glu(355) and Asn(335) and a return of Trp(336) to an optimal position for ligand stacking. The structures of two catalytic mutants of AgaA(A355E) complexed with raffinose and stachyose show that the binding interactions are stronger at subsite -1 to enable the binding of various alpha-galactosides.
The molecular mechanism of thermostable alpha-galactosidases AgaA and AgaB explained by x-ray crystallography and mutational studies.,Merceron R, Foucault M, Haser R, Mattes R, Watzlawick H, Gouet P J Biol Chem. 2012 Nov 16;287(47):39642-52. doi: 10.1074/jbc.M112.394114. Epub, 2012 Sep 25. PMID:23012371<ref>PMID:23012371</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4fnp" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 14:19, 1 March 2024

Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilusCrystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus

Structural highlights

4fnp is a 4 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.803Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AGAA_GEOSE Hydrolyzes the short-chain alpha-galactosaccharides raffinose and stachyose.[1]

See Also

References

  1. ↑ Merceron R, Foucault M, Haser R, Mattes R, Watzlawick H, Gouet P. The molecular mechanism of thermostable alpha-galactosidases AgaA and AgaB explained by x-ray crystallography and mutational studies. J Biol Chem. 2012 Nov 16;287(47):39642-52. doi: 10.1074/jbc.M112.394114. Epub, 2012 Sep 25. PMID:23012371 doi:http://dx.doi.org/10.1074/jbc.M112.394114

4fnp, resolution 2.80Å

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